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Title: Construction, purification, and characterization of anti-BAFF scFv-Fc fusion antibody expressed in CHO/dhfr- cells. Author: Cao M, Cao P, Yan H, Lu W, Ren F, Hu Y, Zhang S. Journal: Appl Biochem Biotechnol; 2009 Jun; 157(3):562-74. PubMed ID: 19099209. Abstract: Elevated levels of B-cell-activating factor of the tumor necrosis factor family (BAFF) have been implicated in the pathogenesis of autoimmune diseases in human. In this study, we have constructed a vector for the expression of a novel compact antibody composed of anti-BAFF single-chain antibody fragment (scFv) and the Fc region (the hinge region, CH2, and CH3 domains) of human IgG1 in Chinese hamster ovary cells. The scFv-Fc fusion protein, showing spontaneous Fc fragment-mediated homodimerization via disulfide bridges, was affinity-purified on protein A Sepharose from culture supernatant. The scFv-Fc antibody was demonstrated to retain high binding affinity to antigen and prolonged clearance time in blood and to possess some human IgG crystallizable fragment effector functions such as protein A binding and antibody-dependent cellular cytotoxicity. These results suggest that this recombinant antibody may have therapeutic applications in the therapy of autoimmune disorders mediated by BAFF.[Abstract] [Full Text] [Related] [New Search]